text: Reversible inhibitors attach to enzymes with non-covalent interactions such as hydrogen bonds, hydrophobic interactions and ionic bonds. Multiple weak bonds between the inhibitor and the enzyme active site combine to produce strong and specific binding.
  In contrast to irreversible inhibitors, reversible inhibitors generally do not undergo chemical reactions when bound to the enzyme and can be easily removed by dilution or dialysis. A special case is covalent reversible inhibitors that form a chemical bond with the enzyme, but the bond can be cleaved so the inhibition is fully reversible.
  Reversible inhibitors are generally categorized into four types, as introduced by Cleland in 1963. They are classified according to the effect of the inhibitor on the V (maximum reaction rate catalysed by the enzyme) and K (the concentration of substrate resulting in half maximal enzyme activity) as the concentration of the enzyme's substrate is varied.